Reviewed, UniProtKB/Swiss-Prot P38986 (ASPG1_YEAST)

Names and origin

Protein names

Recommended name:
    L-asparaginase 1
    EC=3.5.1.1
Alternative name(s):
    L-asparaginase I
    L-asparagine amidohydrolase I
      Short name=ASP I

Gene names

Name:	ASP1
Ordered Locus Names:	YDR321W
ORF Names:	D9798.6

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-asparagine + H2O = L-aspartate + NH3.
Subunit structure	Homopolymer.
Subcellular location	Cytoplasm.
Induction	Expressed constitutively.
Miscellaneous	Yeast contains two L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.
Sequence similarities	Belongs to the asparaginase 1 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	asparagine catabolic process Inferred from genetic interaction. Source: SGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	asparaginase activity Inferred from electronic annotation. Source: EC identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-3014,EBI-3014

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 381	381	L-asparaginase 1		PRO_0000171091
Sites
	Active site	64	1	By similarity
	Active site	141	1	By similarity
	Active site	142	1	By similarity
	Active site	215	1	By similarity
Amino acid modifications
	Modified residue	223	1	Phosphoserine Ref.3
	Modified residue	350	1	Phosphoserine Ref.3
Experimental info
	Mutagenesis	176	1	A → V: Almost no activity.

Sequences

	Sequence		Length	Mass (Da)
	P38986-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 8204CB7C58B5B75F	FASTA	381	41,395
	10 20 30 40 50 60 MKSDSVEITT ICPDVENSQF VVQSNCPETI PEILKSQNAA VNGSGIACQQ RSLPRIKILG 70 80 90 100 110 120 TGGTIASKAI DSSQTAGYHV DLTIQDLLDA IPDISKVCDI EYEQLCNVDS KDINEDILYK 130 140 150 160 170 180 IYKGVSESLQ AFDGIVITHG TDTLSETAFF IESTIDAGDV PIVFVGSMRP STSVSADGPM 190 200 210 220 230 240 NLYQAICIAS NPKSRGRGVL VSLNDQISSG YYITKTNANS LDSFNVRQGY LGNFVNNEIH 250 260 270 280 290 300 YYYPPVKPQG CHKFKLRVDG KHFKLPEVCI LYAHQAFPPA IVNLVADKYD GIVLATMGAG 310 320 330 340 350 360 SLPEEVNETC MKLSLPIVYS KRSMDGMVPI ANVPKKGSKE DNLIASGYLS PEKSRILLQL 370 380 CLAGNYTLEE IKHVFTGVYG G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular isozyme of L-asparaginase." Sinclair K., Warner J.P., Bonthron D.T. Gene 144:37-43(1994) [PubMed: 8026756] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26786 / X2180-1A.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-350, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z27406 Genomic DNA. Translation: CAA81794.1. U32517 Genomic DNA. Translation: AAB64757.1.
PIR	S48513.
RefSeq	NP_010607.1.
3D structure databases
HSSP	HSSP built from PDB template 1HFW based on UniProtKB P06608.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4030N.
IntAct	P38986. 22 interactions.
STRING	P38986.
Proteomic databases
PeptideAtlas	P38986.
Genome annotation databases
Ensembl	YDR321W; YDR321W; YDR321W; Saccharomyces cerevisiae. [Genome view]
GeneID	851920.
GenomeReviews	Gene locus YDR321W in contig Z71256_GR.
KEGG	sce:YDR321W.
NMPDR	fig|4932.3.peg.1373.
Organism-specific databases
CYGD	YDR321w.
SGD	S000002729. ASP1.
Phylogenomic databases
HOGENOM	P38986.
OMA	VNNEIHY.
Enzyme and pathway databases
BRENDA	3.5.1.1. 250.
Gene expression databases
ArrayExpress	P38986.
Genevestigator	P38986.
GermOnline	YDR321W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004550. AsnASE_II. IPR006034. Asp/Glutamnse. [Graphical view]
PANTHER	PTHR11707. Asp/Glutamnse. 1 hit.
Pfam	PF00710. Asparaginase. 1 hit. [Graphical view]
PRINTS	PR00139. ASNGLNASE.
ProDom	PD003221. Asp/Glutamnse. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00520. asnASE_II. 1 hit.
PROSITE	PS00144. ASN_GLN_ASE_1. 1 hit. PS00917. ASN_GLN_ASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	969962.

Entry information

Entry name

ASPG1_YEAST

Accession

Primary (citable) accession number: P38986

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)